Our laboratory studies the function, structure, and mechanism of action of ATP-dependent proteases, with a focus on the Clp/Hsp100 family, which includes ClpAP and ClpXP. ClpAP and ClpXP are universally expressed in bacterial cells. ClpXP is required for regulation of growth and cell division, various stress responses, adaptation, developmental changes, and programmed cell death. It is also linked to virulence of pathogenic bacteria. So far the major roles played by ClpAP have not been defined. Recognition of appropriate substrates by Clp proteases is accomplished by interaction of short sequence motifs present at either the N-terminus or C-terminus of protein substrates with sites in the chaperone component of the protease. From the initial binding site, substrates are then transferred through the complex to the interior of ClpP where they are degraded. Our studies are directed at identifying the binding sites in ClpX and ClpA that interact directly with the degradation motifs of substrates, defining the pathway and mechanism of translocation through the complex, and understanding the specific steps catalyzed by ATP hydrolysis that coordinate the steps and facilitate the entire process. We are also focused on identifying the endogenous substrates of ClpAP in E. coli and defining the metabolic processes or pathways for which ClpAP is required. Projects involve proteomics and microarray analysis, protein-protein interaction studies, biochemical and enzymatic characterization, mutational studies, and in vivo studies of ClpAP activity and physiological analysis of pathways affected.

This position is subject to a background investigation.


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